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3G4V

Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloropentane bound to the XE4 cavity

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0005737cellular_componentcytoplasm
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0001666biological_processresponse to hypoxia
B0005344molecular_functionoxygen carrier activity
B0005737cellular_componentcytoplasm
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 147
ChainResidue
ATYR50
AHOH171
BLYS96
BASN100
APHE51
AARG53
AHIS69
AHIS101
AARG104
AGLU110
APHE111
ACMO148

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 148
ChainResidue
AMET37
APHE51
AHIS69
ALEU73
AHEM147

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 7CL A 150
ChainResidue
ASER21
ATRP22
AILE25
ALEU36
ALEU122
ATRP135

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
ALYS96
AASN100
BTYR50
BPHE51
BARG53
BHIS69
BHIS101
BARG104
BGLU110
BPHE111
BCMO148
BHOH156
BHOH157

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BMET37
BPHE51
BHIS69
BLEU73
BHEM147

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 7CL B 151
ChainResidue
BSER21
BTRP22
BILE25
BASN32
BVAL121
BLEU122
BTRP135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS101
BHIS101

219140

PDB entries from 2024-05-01

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